True-atomic-resolution insights into the structure and functional role of 
linear chains and low-barrier hydrogen bonds in proteins

Borshchevskiy, Valentin; Kovalev, Kirill; Round, Ekaterina; Efremov, Rouslan; Astashkin, Roman; Bourenkov, Gleb; Bratanov, Dmitry; Balandin, Taras; Chizhov, Igor; Baeken, Christian; Gushchin, Ivan; Kuzmin, Alexander; Alekseev, Alexey; Rogachev, Andrey; Willbold, Dieter; Engelhard, Martin; Bamberg, Ernst; Büldt, Georg; Gordeliy, Valentin

doi:10.1038/s41594-022-00762-2

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True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins

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Bamberg, Ernst
Emeritusgroup Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Borshchevskiy, V., Kovalev, K., Round, E., Efremov, R., Astashkin, R., Bourenkov, G., et al. (2022). True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins. Nature Structural and Molecular Biology, 29(5), 440-450. doi:10.1038/s41594-022-00762-2.

Cite as: https://hdl.handle.net/21.11116/0000-000A-61E1-A

Abstract

Hydrogen bonds are fundamental to the structure and function of biological macromolecules and have been explored in detail. The chains of hydrogen bonds (CHBs) and low-barrier hydrogen bonds (LBHBs) were proposed to play essential roles in enzyme catalysis and proton transport. However, high-resolution structural data from CHBs and LBHBs is limited. The challenge is that their 'visualization' requires ultrahigh-resolution structures of the ground and functionally important intermediate states to identify proton translocation events and perform their structural assignment. Our true-atomic-resolution structures of the light-driven proton pump bacteriorhodopsin, a model in studies of proton transport, show that CHBs and LBHBs not only serve as proton pathways, but also are indispensable for long-range communications, signaling and proton storage in proteins. The complete picture of CHBs and LBHBs discloses their multifunctional roles in providing protein functions and presents a consistent picture of proton transport and storage resolving long-standing debates and controversies.